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[[Image:2pon.jpg|left|200px]]
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{{STRUCTURE_2pon|  PDB=2pon  |  SCENE=  }}
'''Solution structure of the Bcl-xL/Beclin-1 complex'''


==Solution structure of the Bcl-xL/Beclin-1 complex==
<StructureSection load='2pon' size='340' side='right'caption='[[2pon]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pon]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PON FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pon OCA], [https://pdbe.org/2pon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pon RCSB], [https://www.ebi.ac.uk/pdbsum/2pon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pon ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BECN1_HUMAN BECN1_HUMAN] Plays a central role in autophagy. Required for the abcission step in cytokinesis. May play a role in antiviral host defense. Protects against infection by a neurovirulent strain of Sindbis virus.<ref>PMID:20208530</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/po/2pon_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pon ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Beclin-1, originally identified as a Bcl-2 binding protein, is an evolutionarily conserved protein required for autophagy. The direct interaction between Beclin-1 and Bcl-2 or Bcl-xL provides a potential convergence point for apoptosis and autophagy, two programmed cell death processes. Given the functional significance of the interaction between Beclin-1 and Bcl-2/Bcl-xL, we performed detailed biochemical and structural characterizations of this interaction. We demonstrated that the Bcl-xL-binding domain of Beclin-1 contains a BH3 domain. Therefore, Beclin-1 is a new member of the BH3-only family proteins. The structure of Bcl-xL in complex with the Beclin-1 BH3 domain was determined at high resolution by NMR spectroscopy. Although similar to other known BH3 domains, the Beclin-1 BH3 domain displays its own distinct features in the complex with Bcl-xL. Systematic analysis of all known Bcl-xL/BH3 domain complexes helped us to identify the molecular basis underlying the capacity of Bcl-xL to recognize diverse target sequences.


==Overview==
Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1.,Feng W, Huang S, Wu H, Zhang M J Mol Biol. 2007 Sep 7;372(1):223-35. Epub 2007 Jun 30. PMID:17659302<ref>PMID:17659302</ref>
Beclin-1, originally identified as a Bcl-2 binding protein, is an evolutionarily conserved protein required for autophagy. The direct interaction between Beclin-1 and Bcl-2 or Bcl-xL provides a potential convergence point for apoptosis and autophagy, two programmed cell death processes. Given the functional significance of the interaction between Beclin-1 and Bcl-2/Bcl-xL, we performed detailed biochemical and structural characterizations of this interaction. We demonstrated that the Bcl-xL-binding domain of Beclin-1 contains a BH3 domain. Therefore, Beclin-1 is a new member of the BH3-only family proteins. The structure of Bcl-xL in complex with the Beclin-1 BH3 domain was determined at high resolution by NMR spectroscopy. Although similar to other known BH3 domains, the Beclin-1 BH3 domain displays its own distinct features in the complex with Bcl-xL. Systematic analysis of all known Bcl-xL/BH3 domain complexes helped us to identify the molecular basis underlying the capacity of Bcl-xL to recognize diverse target sequences.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2PON is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PON OCA].
</div>
<div class="pdbe-citations 2pon" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1., Feng W, Huang S, Wu H, Zhang M, J Mol Biol. 2007 Sep 7;372(1):223-35. Epub 2007 Jun 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17659302 17659302]
*[[B-cell lymphoma proteins 3D structures|B-cell lymphoma proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Feng, W.]]
[[Category: Feng W]]
[[Category: Huang, S.]]
[[Category: Huang S]]
[[Category: Wu, H.]]
[[Category: Wu H]]
[[Category: Zhang, M.]]
[[Category: Zhang M]]
[[Category: Apoptosis]]
[[Category: Apoptosis inhibitor]]
[[Category: Autophagy]]
[[Category: Bcl-2 family protein]]
[[Category: Beclin-1]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:32:58 2008''

Latest revision as of 09:43, 22 May 2024

Solution structure of the Bcl-xL/Beclin-1 complex

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